2016Cereal ChemistryRequires access

Composition of Proteins Extracted from Two Species of Leguminous Bauhinia Grains

Muthulisi Siwela, Eric O. Amonsou

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Abstract

There is a growing demand for alternative protein sources for industrial applications. Bauhinia are underutilized protein‐rich oilseed legumes primarily grown as ornamental plants. In this study, the composition and structure of proteins extracted from two Bauhinia species, B. galpinii and B. petersiana, were determined in comparison with soya bean. Albumin and globulin (75%) were the major storage proteins of Bauhinia. Albumin content of B. galpinii was substantially high (28%), about twice those of soya and B. petersiana. Bauhinia grains were good sources of lysine (approximately 4 g/100 g of protein). By SDS‐PAGE, Bauhinia proteins showed three major protein bands ranging from 17,000 to 76,000 for both species. Only one subunit (17,000) of the basic glycinin (11S) seemed to be present in Bauhinia compared with soya. Bauhinia proteins had more β‐sheet conformation (42%) than α‐helix (22%). Bauhinia grains may provide a new opportunity of protein for industrial applications.

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What this paper is about

There is a growing demand for alternative protein sources for industrial applications. Bauhinia are underutilized protein‐rich oilseed legumes primarily grown as ornamental plants. In this study, the composition and structure of proteins extracted from two Bauhinia species, B. galpinii and B. petersiana, were determined in comparison with soya bean. Albumin and globulin (75%) were the major storage proteins of Bauhinia. Albumin content of B. galpinii was substantially high (28%), about twice those of soya and B. petersiana. Bauhinia grains were good sources of lysine (approximately 4 g/100 g of protein). By SDS‐PAGE, Bauhinia proteins showed three major protein bands ranging from 17,000 to 76,000 for both species. Only one subunit (17,000) of the basic glycinin (11S) seemed to be present in Bauhinia compared with soya. Bauhinia proteins had more β‐sheet conformation (42%) than α‐helix (22%). Bauhinia grains may provide a new opportunity of protein for industrial applications.

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Available abstract

There is a growing demand for alternative protein sources for industrial applications. Bauhinia are underutilized protein‐rich oilseed legumes primarily grown as ornamental plants. In this study, the composition and structure of proteins extracted from two Bauhinia species, B. galpinii and B. petersiana, were determined in comparison with soya bean. Albumin and globulin (75%) were the major storage proteins of Bauhinia. Albumin content of B. galpinii was substantially high (28%), about twice those of soya and B. petersiana. Bauhinia grains were good sources of lysine (approximately 4 g/100 g of protein). By SDS‐PAGE, Bauhinia proteins showed three major protein bands ranging from 17,000 to 76,000 for both species. Only one subunit (17,000) of the basic glycinin (11S) seemed to be present in Bauhinia compared with soya. Bauhinia proteins had more β‐sheet conformation (42%) than α‐helix (22%). Bauhinia grains may provide a new opportunity of protein for industrial applications.

Key concepts: Bauhinia, Storage protein, Chemistry, Botany, Protein subunit, Composition (language), Lysine, Biology

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